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Database: UniProt
Entry: A5PCS1_9SPHN
LinkDB: A5PCS1_9SPHN
Original site: A5PCS1_9SPHN 
ID   A5PCS1_9SPHN            Unreviewed;       489 AA.
AC   A5PCS1;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   16-JAN-2019, entry version 71.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=ED21_22833 {ECO:0000313|EMBL:EDL48401.1};
OS   Erythrobacter sp. SD-21.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL48401.1, ECO:0000313|Proteomes:UP000005498};
RN   [1] {ECO:0000313|EMBL:EDL48401.1, ECO:0000313|Proteomes:UP000005498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD-21 {ECO:0000313|EMBL:EDL48401.1,
RC   ECO:0000313|Proteomes:UP000005498};
RA   Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the initiation and regulation
CC       of chromosomal replication. Binds to the origin of replication; it
CC       binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC       box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC       phospholipids. {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EDL48401.1}.
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DR   EMBL; ABCG01000006; EDL48401.1; -; Genomic_DNA.
DR   ProteinModelPortal; A5PCS1; -.
DR   STRING; 161528.ED21_22833; -.
DR   EnsemblBacteria; EDL48401; EDL48401; ED21_22833.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   Proteomes; UP000005498; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 3.30.300.180; -; 1.
DR   HAMAP; MF_00377; DnaA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR038454; DnaA_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF2; PTHR30050:SF2; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   Pfam; PF11638; DnaA_N; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00760; Bac_DnaA_C; 1.
DR   SUPFAM; SSF48295; SSF48295; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00362; DnaA; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005498};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005498}.
FT   DOMAIN      185    332       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      397    466       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     193    200       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   489 AA;  54704 MW;  7CE3EC46D1A018B4 CRC64;
     MFVMAKSTSG PLGKRKATDE MEDLDAVNLA ADWADISQGL RKDLGHQLHS QWIKPIQLGK
     IDAETGTLDL FLPTEFSANW VKDRFADRLS LAWKIARSEV RKVAISVHPG RRQVADLRLH
     SDGRRPANDA DTSMMAIGAD TLGDTGFTSS VGLDASLTFA AFVTGEANIL AFNAAQRMAA
     TEKPQFSPLY LKAATGQGKT HLLHAIGHTF LQTHNRSRIF YCSAERFMVE FVQALKANRM
     IEFKARLRSF DLLLVDDIQF IIGKASAQEE LLYTIDALLA EGKRLVFAAD RAPQALDGVE
     PRLLSRLSMG LVADIQPADI ELRKKILHSK LTKFAPLAVP EDVLDFLART ITRNVRELVG
     GLNKLIAYAQ LTGQEVSLQL AEEQLTDILS ANRRRITIDE IQRTVCQFYR IDRSEMSSKR
     RARAVVRPRQ VAMYLSKVLT PRSYPEIGRK FGGRDHSTVI HAVRLIEDLR QRDADMDGDV
     RSLLRQLES
//
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